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<jats:p> Recent results from the crystallographic studies on glycogen phosphorylase <jats:italic>b</jats:italic> at 3 A resolution are reviewed with special reference to other themes of the meeting. The structural similarity of the fold of 150 residues in phosphorylase to that observed in lactate dehydrogenase is discussed and the binding sites for NADH in phosphorylase are described. The binding of the potent inhibitor glucose-1,2-cyclic phosphate to phosphorylase <jats:italic>b</jats:italic> in the crystal has been studied at 3 A resolution. The results are compared with those previously obtained for glucose-1-phosphate and discussed with reference to proposals for a mechanism of catalysis that involves the essential cofactor pyridoxal phosphate. </jats:p>

Original publication

DOI

10.1098/rstb.1981.0057

Type

Journal article

Journal

Philosophical Transactions of the Royal Society of London. B, Biological Sciences

Publisher

The Royal Society

Publication Date

26/06/1981

Volume

293

Pages

23 - 41